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P14488

- BLAB_BACCE

UniProt

P14488 - BLAB_BACCE

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Protein

Beta-lactamase 2

Gene
N/A
Organism
Bacillus cereus
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Can hydrolyze carbapenem compounds.

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.

Cofactori

Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi115 – 1151Zinc 1 By similarity
Metal bindingi117 – 1171Zinc 1 By similarity
Metal bindingi119 – 1191Zinc 2 By similarity
Metal bindingi178 – 1781Zinc 1 By similarity
Metal bindingi197 – 1971Zinc 2 By similarity
Metal bindingi239 – 2391Zinc 2 By similarity

GO - Molecular functioni

  1. beta-lactamase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. antibiotic catabolic process Source: InterPro
  2. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKP14488.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase 2 (EC:3.5.2.6)
Alternative name(s):
Beta-lactamase II
Cephalosporinase
Penicillinase
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi110 – 1101D → N: No change in activity.
Mutagenesisi119 – 1191D → N or E: Inactivates the enzyme.
Mutagenesisi177 – 1771G → E: Inactivates the enzyme.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Add
BLAST
Chaini30 – 256227Beta-lactamase 2PRO_0000016943Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP14488.
SMRiP14488. Positions 37-246.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14488-1 [UniParc]FASTAAdd to Basket

« Hide

MKNTLLKLGV CVSLLGITPF VSTISSVQAE RTVEHKVIKN ETGTISISQL    50
NKNVWVHTEL GYFSGEAVPS NGLVLNTSKG LVLVDSSWDD KLTKELIEMV 100
EKKFKKRVTD VIITHAHADR IGGMKTLKER GIKAHSTALT AELAKKNGYE 150
EPLGDLQSVT NLKFGNMKVE TFYPGKGHTE DNIVVWLPQY QILAGGCLVK 200
SASSKDLGNV ADAYVNEWST SIENVLKRYG NINLVVPGHG EVGDRGLLLH 250
TLDLLK 256
Length:256
Mass (Da):28,038
Last modified:January 1, 1990 - v1
Checksum:i670F62378C355C2D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19530 Genomic DNA. Translation: AAA22562.1.
PIRiA32017.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19530 Genomic DNA. Translation: AAA22562.1 .
PIRi A32017.

3D structure databases

ProteinModelPortali P14488.
SMRi P14488. Positions 37-246.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL1744488.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P14488.

Family and domain databases

Gene3Di 3.60.15.10. 1 hit.
InterProi IPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[Graphical view ]
Pfami PF00753. Lactamase_B. 1 hit.
[Graphical view ]
SMARTi SM00849. Lactamase_B. 1 hit.
[Graphical view ]
SUPFAMi SSF56281. SSF56281. 1 hit.
PROSITEi PS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 beta-lactamase II structural gene."
    Lim H.M., Pene J.J., Shaw R.W.
    J. Bacteriol. 170:2873-2878(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 5/B/6.
  2. "Mutations affecting the catalytic activity of Bacillus cereus 5/B/6 beta-lactamase II."
    Lim H.M., Pene J.J.
    J. Biol. Chem. 264:11682-11687(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  3. "Site-directed mutagenesis of dicarboxylic acids near the active site of Bacillus cereus 5/B/6 beta-lactamase II."
    Lim H.M., Iyer R.K., Pene J.J.
    Biochem. J. 276:401-404(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

Entry informationi

Entry nameiBLAB_BACCE
AccessioniPrimary (citable) accession number: P14488
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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